PXD013476

PXD013476 is an original dataset announced via ProteomeXchange.

Title	Effects of a phosphomimetic mutation and nucleotide binding on the interaction of Hsp90a with co-chaperone Aha1 analyzed by chemical cross-linking with mass spectrometry
Description	Complex conformational dynamics are essential for the chaperone function of heat shock protein 90 (Hsp90), including transient, ATP-biased N-domain dimerization establishing ATPase competence. Biochemical data demonstrate that the intrinsic, but weak, ATP hydrolyzing activity of Hsp90 is markedly enhanced by the co-chaperone Aha1. However, cellular concentration of Aha1 is substoichiometric relative to Hsp90. In cells, interaction of this important co-chaperone with Hsp90 is up-regulated by posttranslational modifications (PTMs), including phosphorylation of a highly conserved tyrosine (Y313 in Hsp90a). Here we use chemical cross-linking with mass spectrometry to explore the the impacts of a phosphomimetic mutation (Y313E) and binding of a non-hydrolyzable ATP analog (AMP-PNP),on the structure Hsp90a and its interaction with Aha1.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:55:17.485.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Juan Chavez
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ FT; Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-04-12 01:53:58	ID requested
1	2019-06-17 03:21:48	announced
⏵ 2	2024-10-22 04:55:22	announced	2024-10-22: Updated project metadata.

Xu W, Beebe K, Chavez JD, Boysen M, Lu Y, Zuehlke AD, Keramisanou D, Trepel JB, Prodromou C, Mayer MP, Bruce JE, Gelis I, Neckers L, Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1. Nat Commun, 10(1):2574(2019) [pubmed]

10.1038/s41467-019-10463-y;

submitter keyword: cross-linking, Aha1, PTM,heat shock, phosphorylation, XL-MS, chaperone, Hsp90

Len Neckers
contact affiliation	Urologic Oncology Branch, National Cancer Institute, Bethesda, MD 20892, USA
contact email	neckersl@mail.nih.gov
lab head
Juan Chavez
contact affiliation	University of Washington
contact email	jdchavez@uw.edu
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/06/PXD013476

PRIDE project URI

• PRIDE
  1. PXD013476
     1. Label: PRIDE project
     2. Name: Effects of a phosphomimetic mutation and nucleotide binding on the interaction of Hsp90a with co-chaperone Aha1 analyzed by chemical cross-linking with mass spectrometry